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Protein

EGF-like repeat and discoidin I-like domain-containing protein 3

Gene

Edil3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191CalciumBy similarity
Metal bindingi120 – 1201Calcium; via carbonyl oxygenBy similarity
Metal bindingi122 – 1221CalciumBy similarity
Metal bindingi136 – 1361CalciumBy similarity
Metal bindingi137 – 1371Calcium; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
EGF-like repeat and discoidin I-like domain-containing protein 3
Alternative name(s):
Developmentally-regulated endothelial cell locus 1 protein
Integrin-binding protein DEL1
Gene namesi
Name:Edil3
Synonyms:Del1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1329025. Edil3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 480457EGF-like repeat and discoidin I-like domain-containing protein 3PRO_0000007523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 37By similarity
Disulfide bondi31 ↔ 48By similarity
Disulfide bondi50 ↔ 59By similarity
Glycosylationi73 – 731O-linked (GalNAc...)By similarity
Disulfide bondi78 ↔ 89By similarity
Disulfide bondi83 ↔ 105By similarity
Glycosylationi88 – 881O-linked (Fuc...)By similarity
Disulfide bondi107 ↔ 116By similarity
Disulfide bondi123 ↔ 134By similarity
Disulfide bondi128 ↔ 143By similarity
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi145 ↔ 154By similarity
Disulfide bondi158 ↔ 314By similarity
Disulfide bondi301 ↔ 305By similarity
Disulfide bondi319 ↔ 476By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO35474.
PaxDbiO35474.
PRIDEiO35474.

PTM databases

PhosphoSiteiO35474.

Expressioni

Tissue specificityi

Expressed in angioblasts and early endothelial cells. By embryonic day 13.5, also expressed in a restricted group of non-endothelial cells including chondrocytes and retinal neurons.

Developmental stagei

Expressed in the embryo from day 7. After day 15.5, expression decreases and disappears completely by the time of birth.

Gene expression databases

BgeeiO35474.
CleanExiMM_EDIL3.
ExpressionAtlasiO35474. baseline and differential.
GenevisibleiO35474. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000080462.

Structurei

3D structure databases

ProteinModelPortaliO35474.
SMRiO35474. Positions 26-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6037EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini74 – 11744EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 15537EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 314157F5/8 type C 1PROSITE-ProRule annotationAdd
BLAST
Domaini319 – 476158F5/8 type C 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 983Cell attachment siteBy similarity

Domaini

EGF2 and EGF3 form a rigid rod via an interdomain calcium ion binding site, while the long linker between EGF1 and EGF2 lends considerable flexibility to EGF1.By similarity

Sequence similaritiesi

Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IFBC. Eukaryota.
ENOG41114BV. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000236278.
HOVERGENiHBG002385.
InParanoidiO35474.
OMAiNINECEA.
TreeFamiTF330156.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR029828. EDIL-3.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF29. PTHR10127:SF29. 2 hits.
PfamiPF00008. EGF. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 3 hits.
SM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 3 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 1 hit.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35474-1) [UniParc]FASTAAdd to basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKHLVAAWLL VGLSLGVPQF GKGDICNPNP CENGGICLSG LADDSFSCEC
60 70 80 90 100
PEGFAGPNCS SVVEVASDEE KPTSAGPCIP NPCHNGGTCE ISEAYRGDTF
110 120 130 140 150
IGYVCKCPRG FNGIHCQHNI NECEAEPCRN GGICTDLVAN YSCECPGEFM
160 170 180 190 200
GRNCQYKCSG PLGIEGGIIS NQQITASSTH RALFGLQKWY PYYARLNKKG
210 220 230 240 250
LINAWTAAEN DRWPWIQINL QRKMRVTGVI TQGAKRIGSP EYIKSYKIAY
260 270 280 290 300
SNDGKTWAMY KVKGTNEEMV FRGNVDNNTP YANSFTPPIK AQYVRLYPQI
310 320 330 340 350
CRRHCTLRME LLGCELSGCS EPLGMKSGHI QDYQITASSV FRTLNMDMFT
360 370 380 390 400
WEPRKARLDK QGKVNAWTSG HNDQSQWLQV DLLVPTKVTG IITQGAKDFG
410 420 430 440 450
HVQFVGSYKL AYSNDGEHWM VHQDEKQRKD KVFQGNFDND THRKNVIDPP
460 470 480
IYARFIRILP WSWYGRITLR SELLGCAEEE
Length:480
Mass (Da):53,712
Last modified:July 27, 2011 - v2
Checksum:i10DBA65C19F1C70F
GO
Isoform 2 (identifier: O35474-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     218-221: INLQ → VTVG
     222-480: Missing.

Show »
Length:221
Mass (Da):23,751
Checksum:i45F77DB8EDABBDD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871Q → R in AAB86585 (PubMed:9420328).Curated
Sequence conflicti187 – 1871Q → R in AAB86586 (PubMed:9420328).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei218 – 2214INLQ → VTVG in isoform 2. 1 PublicationVSP_050400
Alternative sequencei222 – 480259Missing in isoform 2. 1 PublicationVSP_050401Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031524 mRNA. Translation: AAB86585.1.
AF031525 mRNA. Translation: AAB86586.1.
AK036117 mRNA. Translation: BAC29310.1.
AK139093 mRNA. Translation: BAE23887.1.
CT010458
, AC121916, AC154668, AC161244 Genomic DNA. Translation: CAO91806.1.
CH466567 Genomic DNA. Translation: EDL00986.1.
BC056386 mRNA. Translation: AAH56386.1.
CCDSiCCDS26669.1. [O35474-1]
RefSeqiNP_001033076.1. NM_001037987.3. [O35474-1]
NP_034233.1. NM_010103.4.
UniGeneiMm.125580.

Genome annotation databases

EnsembliENSMUST00000081769; ENSMUSP00000080462; ENSMUSG00000034488. [O35474-1]
GeneIDi13612.
KEGGimmu:13612.
UCSCiuc007rjb.2. mouse. [O35474-2]
uc007rjd.2. mouse. [O35474-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031524 mRNA. Translation: AAB86585.1.
AF031525 mRNA. Translation: AAB86586.1.
AK036117 mRNA. Translation: BAC29310.1.
AK139093 mRNA. Translation: BAE23887.1.
CT010458
, AC121916, AC154668, AC161244 Genomic DNA. Translation: CAO91806.1.
CH466567 Genomic DNA. Translation: EDL00986.1.
BC056386 mRNA. Translation: AAH56386.1.
CCDSiCCDS26669.1. [O35474-1]
RefSeqiNP_001033076.1. NM_001037987.3. [O35474-1]
NP_034233.1. NM_010103.4.
UniGeneiMm.125580.

3D structure databases

ProteinModelPortaliO35474.
SMRiO35474. Positions 26-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000080462.

PTM databases

PhosphoSiteiO35474.

Proteomic databases

MaxQBiO35474.
PaxDbiO35474.
PRIDEiO35474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081769; ENSMUSP00000080462; ENSMUSG00000034488. [O35474-1]
GeneIDi13612.
KEGGimmu:13612.
UCSCiuc007rjb.2. mouse. [O35474-2]
uc007rjd.2. mouse. [O35474-1]

Organism-specific databases

CTDi10085.
MGIiMGI:1329025. Edil3.

Phylogenomic databases

eggNOGiENOG410IFBC. Eukaryota.
ENOG41114BV. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000236278.
HOVERGENiHBG002385.
InParanoidiO35474.
OMAiNINECEA.
TreeFamiTF330156.

Miscellaneous databases

ChiTaRSiEdil3. mouse.
PROiO35474.
SOURCEiSearch...

Gene expression databases

BgeeiO35474.
CleanExiMM_EDIL3.
ExpressionAtlasiO35474. baseline and differential.
GenevisibleiO35474. MM.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR029828. EDIL-3.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF29. PTHR10127:SF29. 2 hits.
PfamiPF00008. EGF. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 3 hits.
SM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 3 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 1 hit.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of developmental endothelial locus-1: an embryonic endothelial cell protein that binds the alphavbeta3 integrin receptor."
    Hidai C., Zupancic T.J., Penta K., Mikhail A., Kawana M., Quertermous E.E., Aoka Y., Fukagawa M., Matsui Y., Platika D., Auerbach R., Hogan B.L.M., Snodgrass R., Quertermous T.
    Genes Dev. 12:21-33(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiEDIL3_MOUSE
AccessioniPrimary (citable) accession number: O35474
Secondary accession number(s): O35475, Q8CBF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.